5IQZ
Crystal structure of N-terminal domain of Human SIRT7
Summary for 5IQZ
Entry DOI | 10.2210/pdb5iqz/pdb |
Related PRD ID | PRD_900001 |
Descriptor | SIRT7 protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
Functional Keywords | sirt7, fusion protein, maltose binding, alpha histone deacetylase sirtuin, sugar binding protein |
Biological source | Homo sapiens |
Total number of polymer chains | 1 |
Total formula weight | 49506.05 |
Authors | Thakur, K.G.,Priyanka, A. (deposition date: 2016-03-11, release date: 2016-07-27, Last modification date: 2023-11-08) |
Primary citation | Priyanka, A.,Solanki, V.,Parkesh, R.,Thakur, K.G. Crystal structure of the N-terminal domain of human SIRT7 reveals a three-helical domain architecture Proteins, 84:1558-1563, 2016 Cited by PubMed Abstract: Human SIRT7 is an NAD(+) dependent deacetylase, which belongs to sirtuin family of proteins. SIRT7, like other sirtuins has conserved catalytic domain and is flanked by N- and C-terminal domains reported to play vital functional roles. Here, we report the crystal structure of the N-terminal domain of human SIRT7 (SIRT7(NTD) ) at 2.3 Å resolution as MBP-SIRT7(NTD) fusion protein. SIRT7(NTD) adopts three-helical domain architecture and comparative structural analyses suggest similarities to some DNA binding motifs and transcription regulators. We also report here the importance of N- and C-terminal domains in soluble expression of SIRT7. Proteins 2016; 84:1558-1563. © 2016 Wiley Periodicals, Inc. PubMed: 27287224DOI: 10.1002/prot.25085 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.334 Å) |
Structure validation
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